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P24472 (GSTA4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase A4

EC=2.5.1.18
Alternative name(s):
GST A4-4
Short name=GSTA4-4
GST class-alpha member 4
Glutathione S-transferase 5.7
Short name=GST 5.7
Gene names
Name:Gsta4
Synonyms:Gsta
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Ref.6

Catalytic activity

RX + glutathione = HX + R-S-glutathione. Ref.6

Subunit structure

Homodimer. Ref.6

Subcellular location

Cytoplasm.

Post-translational modification

The N-terminus is blocked.

Miscellaneous

On the basis of immunological and kinetics data, GST 5.7 is distinct from alpha, mu and pI classes of GTS. However it has been postulated that this protein may be part of a distinct subgroup within this alpha class.

The variations were found from AA sequencing and imply there are multiple forms of this protein. These variations are likely to be sex-linked and tissue specific.

Sequence similarities

Belongs to the GST superfamily. Alpha family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   Molecular functionTransferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processglutathione metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione transferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 222222Glutathione S-transferase A4
PRO_0000185791

Regions

Domain3 – 8381GST N-terminal
Domain85 – 208124GST C-terminal
Region54 – 552Glutathione binding
Region67 – 682Glutathione binding

Sites

Binding site91Glutathione By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Natural variations

Natural variant1151K → P Requires 2 nucleotide substitutions.
Natural variant1671V → G.
Natural variant179 – 1802PL → GE.

Experimental info

Sequence conflict361E → D in BAB31640. Ref.2
Sequence conflict205 – 2062KP → SA in BAB27873. Ref.2
Sequence conflict2181T → I in AAA37754. Ref.1

Secondary structure

....................................... 222
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P24472 [UniParc].

Last modified January 23, 2002. Version 3.
Checksum: B580E3415289424D

FASTA22225,564
        10         20         30         40         50         60 
MAAKPKLYYF NGRGRMESIR WLLAAAGVEF EEEFLETREQ YEKMQKDGHL LFGQVPLVEI 

        70         80         90        100        110        120 
DGMMLTQTRA ILSYLAAKYN LYGKDLKERV RIDMYADGTQ DLMMMIAVAP FKTPKEKEES 

       130        140        150        160        170        180 
YDLILSRAKT RYFPVFEKIL KDHGEAFLVG NQLSWADIQL LEAILMVEEL SAPVLSDFPL 

       190        200        210        220 
LQAFKTRISN IPTIKKFLQP GSQRKPPPDG PYVEVVRTVL KF 

« Hide

References

« Hide 'large scale' references
[1]"A subgroup of class alpha glutathione S-transferases. Cloning of cDNA for mouse lung glutathione S-transferase GST 5.7."
Zimniak P., Eckles M.A., Saxena M., Awasthi Y.C.
FEBS Lett. 313:173-176(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo, Small intestine and Tongue.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Characterization of a novel glutathione S-transferase isoenzyme from mouse lung and liver having structural similarity to rat glutathione S-transferase 8-8."
Medh R.D., Saxena M., Singhal S.S., Ahmad H., Awasthi Y.C.
Biochem. J. 278:793-799(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 106-120 AND 167-184.
Strain: CD-1.
Tissue: Liver and Lung.
[5]"Crystal structure of a murine alpha-class glutathione S-transferase involved in cellular defense against oxidative stress."
Krengel U., Schroter K.H., Hoier H., Arkema A., Kalk K.H., Zimniak P., Dijkstra B.W.
FEBS Lett. 422:285-290(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
Tissue: Lung.
[6]"Crystal structure of a murine glutathione S-transferase in complex with a glutathione conjugate of 4-hydroxynon-2-enal in one subunit and glutathione in the other: evidence of signaling across the dimer interface."
Xiao B., Singh S.P., Nanduri B., Awasthi Y.C., Zimniak P., Ji X.
Biochemistry 38:11887-11894(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT.
Tissue: Lung.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L06047 mRNA. Translation: AAA37754.1.
AK008189 mRNA. Translation: BAB25520.1.
AK008193 mRNA. Translation: BAB25524.1.
AK008400 mRNA. Translation: BAB25649.1.
AK008490 mRNA. Translation: BAB25696.1.
AK009668 mRNA. Translation: BAB26429.1.
AK010098 mRNA. Translation: BAB26701.1.
AK011177 mRNA. Translation: BAB27449.1.
AK011841 mRNA. Translation: BAB27873.1.
AK019100 mRNA. Translation: BAB31546.1.
AK019271 mRNA. Translation: BAB31640.1.
BC012639 mRNA. Translation: AAH12639.1.
CCDSCCDS23357.1.
PIRS27234.
RefSeqNP_034487.2. NM_010357.3.
UniGeneMm.2662.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B48X-ray2.60A/B2-222[»]
1GUKX-ray2.90A/B1-222[»]
ProteinModelPortalP24472.
SMRP24472. Positions 2-222.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP24472. 2 interactions.
MINTMINT-1487605.

Chemistry

DrugBankDB00143. Glutathione.

PTM databases

PhosphoSiteP24472.

2D gel databases

REPRODUCTION-2DPAGEP24472.

Proteomic databases

MaxQBP24472.
PaxDbP24472.
PRIDEP24472.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034903; ENSMUSP00000034903; ENSMUSG00000032348.
GeneID14860.
KEGGmmu:14860.
UCSCuc009qty.2. mouse.

Organism-specific databases

CTD2941.
MGIMGI:1309515. Gsta4.

Phylogenomic databases

eggNOGNOG266414.
GeneTreeENSGT00670000097856.
HOGENOMHOG000115734.
HOVERGENHBG053749.
InParanoidP24472.
KOK00799.
OMAMGMIMYL.
OrthoDBEOG79CZ0K.
PhylomeDBP24472.
TreeFamTF105321.

Gene expression databases

BgeeP24472.
CleanExMM_GSTA4.
GenevestigatorP24472.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01266. GSTRNSFRASEA.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP24472.
NextBio287101.
PROP24472.
SOURCESearch...

Entry information

Entry nameGSTA4_MOUSE
AccessionPrimary (citable) accession number: P24472
Secondary accession number(s): Q9CQ81 expand/collapse secondary AC list , Q9CTY7, Q9CY87, Q9D038
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2002
Last modified: July 9, 2014
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot